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The role of phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, in the regulation of carbon metabolism in gram-positive bacteria

✍ Scribed by Jonathan Reizer; Antonio H. Romano; Josef Deutscher

Publisher: John Wiley and Sons
Year: 1993
Tongue: English
Weight: 626 KB
Volume: 51
Category: Article
ISSN: 0730-2312
DOI: 10.1002/jcb.240510105

No coin nor oath required. For personal study only.

✦ Synopsis

HPr of the Gram-positive bacterial phosphotransferase system (PTS) can be phosphorylated by an ATP-dependent protein kinase on a serine residue or by PEP-dependent Enzyme I on a histidyl residue. Both phosphorylation events appear to influence the metabolism of non-PTS carbon sources. Catabolite repression of the gluconate (gnt) operon of 6. subtilis appears to be regulated by the former phosphorylation event, while glycerol kinase appears to be regulated by the latter phosphorylation reaction. The extent of our understanding of these processes will be described.

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